Characterization of a competitive and reversible ligand to E2 conformation of Na, K ATPase molecule.

Abstract:

:The binding of cardiac glycosides to the E2 conformation of Na, K ATPase suggests that this conformation may represent a potential regulatory site for an endogenous ligand. To examine this hypothesis, delipidated and desalted, ethanolic extracts were prepared from plasma. Plasma extracts produced displacement of 3H-ouabain from Type I and II high affinity binding sites that was parallel to the displacement by cold ouabain. Plasma extracts shifted the binding curve of 3H-ouabain to the right indicating a competitive and reversible displacement. Extracts also produced a dose-dependent inhibition of Na, K ATPase and K-stimulated, p-nitrophenyl phosphatase activity. These results indicate that this ligand may function as an endogenous ligand to the E2 conformation of the Na, K ATPase molecule and be involved in its regulation.

authors

Rauch AL,Buckalew VM Jr

doi

10.1016/0006-291x(88)90441-x

subject

Has Abstract

pub_date

1988-01-29 00:00:00

pages

648-54

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(88)90441-X

journal_volume

150

pub_type

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